Atomistry » Copper » PDB 2aps-2cg1 » 2aps
Atomistry »
  Copper »
    PDB 2aps-2cg1 »
      2aps »

Copper in PDB 2aps: Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps was solved by K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.050, 123.880, 107.250, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 26.1

Other elements in 2aps:

The structure of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae (pdb code 2aps). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae, PDB code: 2aps:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2aps

Go back to Copper Binding Sites List in 2aps
Copper binding site 1 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu300

b:41.4
occ:0.50
NE2 A:HIS50 1.7 57.3 1.0
NE2 A:HIS48 1.7 52.7 1.0
CE1 A:HIS50 2.5 58.1 1.0
CE1 A:HIS48 2.7 55.3 1.0
CD2 A:HIS48 2.8 54.2 1.0
CD2 A:HIS50 2.8 55.9 1.0
ND1 A:HIS50 3.6 59.3 1.0
ND1 A:HIS48 3.8 50.8 1.0
CG A:HIS50 3.8 56.3 1.0
CG A:HIS48 3.9 50.4 1.0

Copper binding site 2 out of 4 in 2aps

Go back to Copper Binding Sites List in 2aps
Copper binding site 2 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu402

b:43.8
occ:1.00
NE2 A:HIS141 1.9 37.4 1.0
NE2 A:HIS62 2.2 46.7 1.0
ND1 A:HIS60 2.3 36.3 1.0
CE1 A:HIS141 2.8 41.5 1.0
NE2 A:HIS85 2.9 39.7 1.0
CD2 A:HIS141 3.0 41.2 1.0
CE1 A:HIS62 3.1 45.3 1.0
CE1 A:HIS60 3.2 34.7 1.0
CG A:HIS60 3.2 34.1 1.0
CD2 A:HIS62 3.3 46.8 1.0
CD2 A:HIS85 3.4 37.1 1.0
CB A:HIS60 3.5 33.1 1.0
CE1 A:HIS85 3.8 38.1 1.0
CB A:MET139 3.9 47.4 1.0
ND1 A:HIS141 3.9 39.9 1.0
CG A:MET139 4.0 50.6 1.0
CG A:HIS141 4.1 39.6 1.0
ND1 A:HIS62 4.3 47.4 1.0
NE2 A:HIS60 4.3 35.2 1.0
CD2 A:HIS60 4.3 34.7 1.0
CG A:HIS62 4.4 45.1 1.0
CG A:HIS85 4.4 39.1 1.0
CA A:HIS60 4.5 34.4 1.0
N A:HIS60 4.6 33.9 1.0
O A:HOH1271 4.6 47.3 1.0
ND1 A:HIS85 4.6 37.6 1.0
O A:HIS60 4.7 39.0 1.0
C A:HIS60 4.8 36.5 1.0
O A:MET139 4.9 43.0 1.0

Copper binding site 3 out of 4 in 2aps

Go back to Copper Binding Sites List in 2aps
Copper binding site 3 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu500

b:32.4
occ:1.00
O B:HOH1353 1.5 32.4 1.0
NE2 B:HIS48 2.3 34.5 1.0
NE2 B:HIS50 2.3 24.1 1.0
CD2 B:HIS50 3.0 22.9 1.0
CE1 B:HIS48 3.1 35.8 1.0
CD2 B:HIS48 3.2 32.4 1.0
CE1 B:HIS50 3.5 24.0 1.0
ND1 B:HIS48 4.2 37.1 1.0
CG B:HIS50 4.2 22.7 1.0
CG B:HIS48 4.3 30.0 1.0
ND1 B:HIS50 4.4 26.9 1.0

Copper binding site 4 out of 4 in 2aps

Go back to Copper Binding Sites List in 2aps
Copper binding site 4 out of 4 in the Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Cu/Zn Superoxide Dismutase From Actinobacillus Pleuropneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu602

b:26.6
occ:1.00
ND1 B:HIS60 2.0 21.3 1.0
NE2 B:HIS62 2.1 18.0 1.0
NE2 B:HIS141 2.1 23.9 1.0
CE1 B:HIS60 2.8 22.3 1.0
CE1 B:HIS62 3.0 19.1 1.0
NE2 B:HIS85 3.0 20.6 1.0
CD2 B:HIS141 3.0 21.6 1.0
CD2 B:HIS62 3.1 18.9 1.0
CG B:HIS60 3.1 21.2 1.0
O B:HOH1224 3.1 41.5 1.0
CE1 B:HIS141 3.1 22.1 1.0
CD2 B:HIS85 3.5 21.7 1.0
CB B:HIS60 3.6 20.6 1.0
CE1 B:HIS85 3.9 20.4 1.0
CB B:MET139 3.9 20.2 1.0
NE2 B:HIS60 4.0 25.2 1.0
CG B:MET139 4.0 22.7 1.0
ND1 B:HIS62 4.1 19.7 1.0
CD2 B:HIS60 4.1 19.6 1.0
CG B:HIS141 4.2 18.6 1.0
CG B:HIS62 4.2 21.5 1.0
ND1 B:HIS141 4.2 18.7 1.0
O B:HOH1223 4.3 25.4 1.0
CG B:HIS85 4.4 22.1 1.0
CA B:HIS60 4.5 19.7 1.0
N B:HIS60 4.5 21.1 1.0
ND1 B:HIS85 4.6 21.4 1.0
O B:HIS60 4.7 18.2 1.0
C B:HIS60 4.8 20.7 1.0
O B:MET139 4.9 19.9 1.0

Reference:

K.T.Forest, P.R.Langford, J.S.Kroll, E.D.Getzoff. Cu,Zn Superoxide Dismutase Structure From A Microbial Pathogen Establishes A Class with A Conserved Dimer Interface. J.Mol.Biol. V. 296 145 2000.
ISSN: ISSN 0022-2836
PubMed: 10656823
DOI: 10.1006/JMBI.1999.3448
Page generated: Sun Dec 13 11:03:32 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy